Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Homodimer and heterodimer with PRMT8. The dimer can then associate to form a homohexamer. Interacts with ILF3, BTG1, BTG2, SUPT5H and interferon-alpha/beta receptor 1. Interacts with NFATC2IP. Widely expressed. By BTG1, BTG2 and ILF3. Belongs to the protein arginine N-methyltransferase family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 126.96.36.199; Methyltransferase; Methyltransferase, protein arginine; Nuclear receptor co-regulator
Molecular Function: enzyme binding; histone methyltransferase activity; identical protein binding; methyl-CpG binding; methyltransferase activity; mitogen-activated protein kinase p38 binding; N-methyltransferase activity; protein binding; protein methyltransferase activity; protein-arginine N-methyltransferase activity; protein-arginine omega-N asymmetric methyltransferase activity
Biological Process: cell surface receptor linked signal transduction; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; histone methylation; negative regulation of megakaryocyte differentiation; neurite development; peptidyl-arginine methylation; positive regulation of erythrocyte differentiation; positive regulation of hemoglobin biosynthetic process; protein amino acid methylation; regulation of transcription, DNA-dependent